Michael M. Mbughuni, Ph.D.
Affiliations: | 2012 | Biochemistry, Molecular Bio, and Biophysics | University of Minnesota, Twin Cities, Minneapolis, MN |
Area:
oxygenasesGoogle:
"Michael Mbughuni"Mean distance: 11.29 | S | N | B | C | P |
Parents
Sign in to add mentorJohn D. Lipscomb | grad student | 2012 | UMN | |
(Kinetic, spectroscopic, and mutagenesis studies of homoprotocatechuate 2,3-dioxygenase.) |
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Publications
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Sutherlin KD, Wasada-Tsutsui Y, Mbughuni MM, et al. (2018) NRVS definition of O intermediates in an extradiol dioxygenase: correlation to crystallography and reactivity. Journal of the American Chemical Society |
McAndrew RP, Sathitsuksanoh N, Mbughuni MM, et al. (2017) Reply to Kiser: Dioxygen binding in NOV1 crystal structures. Proceedings of the National Academy of Sciences of the United States of America |
McAndrew RP, Sathitsuksanoh N, Mbughuni MM, et al. (2016) Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase. Proceedings of the National Academy of Sciences of the United States of America |
Meier KK, Rogers MS, Kovaleva EG, et al. (2015) A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorganic Chemistry. 54: 10269-80 |
Mbughuni MM, Meier KK, Münck E, et al. (2012) Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant. Biochemistry. 51: 8743-54 |
Mbughuni MM, Chakrabarti M, Hayden JA, et al. (2011) Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates. Biochemistry. 50: 10262-74 |
Mbughuni MM, Chakrabarti M, Hayden JA, et al. (2010) Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proceedings of the National Academy of Sciences of the United States of America. 107: 16788-93 |